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Träfflista för sökning "WFRF:(Elofsson Arne 1966 ) srt2:(2013-2014)"

Sökning: WFRF:(Elofsson Arne 1966 ) > (2013-2014)

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1.
  • Light, Sara, et al. (författare)
  • The impact of splicing on protein domain architecture
  • 2013
  • Ingår i: Current opinion in structural biology. - : Elsevier BV. - 0959-440X .- 1879-033X. ; 23:3, s. 451-458
  • Tidskriftsartikel (refereegranskat)abstract
    • Many proteins are composed of protein domains, functional units of common descent. Multidomain forms are common in all eukaryotes making up more than half of the proteome and the evolution of novel domain architecture has been accelerated in metazoans. It is also becoming increasingly clear that alternative splicing is prevalent among vertebrates. Given that protein domains are defined as structurally, functionally and evolutionarily distinct units, one may speculate that some alternative splicing events may lead to clean excisions of protein domains, thus generating a number of different domain architectures from one gene template. However, recent findings indicate that smaller alternative splicing events, in particular in disordered regions, might be more prominent than domain architectural changes.The problem of identifying protein isoforms is, however, still not resolved. Clearly, many splice forms identified through detection of mRNA sequences appear to produce 'nonfunctional' proteins, such as proteins with missing internal secondary structure elements. Here, we review the state of the art methods for identification of functional isoforms and present a summary of what is known, thus far, about alternative splicing with regard to protein domain architectures.
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2.
  • Michel, Mirco, et al. (författare)
  • PconsFold : improved contact predictions improve protein models
  • 2014
  • Ingår i: Bioinformatics. - : Oxford University Press (OUP). - 1367-4803 .- 1367-4811. ; 30:17, s. 1482-1488
  • Tidskriftsartikel (refereegranskat)abstract
    • Motivation: Recently it has been shown that the quality of protein contact prediction from evolutionary information can be improved significantly if direct and indirect information is separated. Given sufficiently large protein families, the contact predictions contain sufficient information to predict the structure of many protein families. However, since the first studies contact prediction methods have improved. Here, we ask how much the final models are improved if improved contact predictions are used.Results: In a small benchmark of 15 proteins, we show that the TM-scores of top-ranked models are improved by on average 33% using PconsFold compared with the original version of EVfold. In a larger benchmark, we find that the quality is improved with 15-30% when using PconsC in comparison with earlier contact prediction methods. Further, using Rosetta instead of CNS does not significantly improve global model accuracy, but the chemistry of models generated with Rosetta is improved.
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3.
  • Skwark, Marcin J., et al. (författare)
  • PconsC : combination of direct information methods and alignments improves contact prediction
  • 2013
  • Ingår i: Bioinformatics. - : Oxford University Press (OUP). - 1367-4803 .- 1367-4811. ; 29:14, s. 1815-1816
  • Tidskriftsartikel (refereegranskat)abstract
    • Recently, several new contact prediction methods have been published. They use (i) large sets of multiple aligned sequences and (ii) assume that correlations between columns in these alignments can be the results of indirect interaction. These methods are clearly superior to earlier methods when it comes to predicting contacts in proteins. Here, we demonstrate that combining predictions from two prediction methods, PSICOV and plmDCA, and two alignment methods, HHblits and jackhmmer at four different e-value cut-offs, provides a relative improvement of 20% in comparison with the best single method, exceeding 70% correct predictions for one contact prediction per residue.
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  • Resultat 1-3 av 3
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tidskriftsartikel (3)
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refereegranskat (3)
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Elofsson, Arne, 1966 ... (3)
Skwark, Marcin J. (2)
Abdel-Rehim, Abbi (1)
Sander, Chris (1)
Light, Sara (1)
Hayat, Sikander (1)
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Marks, Debora S. (1)
Michel, Mirco (1)
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Stockholms universitet (3)
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